• Journal of Microbiology and Biotechnology
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• v.11 no.2
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• pp.337-341
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• 2001

To isolate antifungal substances from Korean radish (Raphanus Sativus L.) seeds, various purification techniques such as DE52 cellulose anion exchange, SP-Sephadex C-25 cation exchange, and Sephadex G-50 gel filtration chromatographies were used. The molecular masses of two purified R. sativus antifungal proteins (RAPs) were estimated to be about 6.1 kDa (RAP-1) and 6.2 kDa (RAP-2) by SDS-PAGE, and 5.8 kDa(RAP-1) and 6.2 kDa (RAP-2 by a gel filtration chromatography, respectively. Purified proteins RAP-1 and 2 clearly exhibited different growth inhibitory activities against other microorganisms like Candida albicans and Saccharomyces cerevisiae. Although they have similar molecular masses, both RAP-1 and 2 proteins are not identical because their microbial inhibitory actions were different. Therefore, RAP-1 could be a new antifungal protein when compared with the antifungal activities of 2S albumins, Rs-AFPs, Mj-AMPs, chitinase, glucanase, permatin, and ribosome inactivating proteins, all of which are anifungal proteins of plants.